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Yorodumi- PDB-6r1a: Cereblon isoform 4 from Magnetospirillum gryphiswaldense in compl... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6r1a | ||||||
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Title | Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex with compound 20b | ||||||
Components | Cereblon isoform 4 | ||||||
Keywords | SIGNALING PROTEIN / proteolysis targeting chimera / PROTAC / protein degradation | ||||||
Function / homology | CULT domain / CULT domain profile. / metal ion binding / S-Thalidomide / Chem-JP8 / PHOSPHATE ION / Cereblon isoform 4 Function and homology information | ||||||
Biological species | Magnetospirillum gryphiswaldense MSR-1 (magnetotactic) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.54 Å | ||||||
Authors | Heim, C. / Hartmann, M.D. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2019 Title: De-Novo Design of Cereblon (CRBN) Effectors Guided by Natural Hydrolysis Products of Thalidomide Derivatives. Authors: Heim, C. / Pliatsika, D. / Mousavizadeh, F. / Bar, K. / Hernandez Alvarez, B. / Giannis, A. / Hartmann, M.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6r1a.cif.gz | 157 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6r1a.ent.gz | 123 KB | Display | PDB format |
PDBx/mmJSON format | 6r1a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r1/6r1a ftp://data.pdbj.org/pub/pdb/validation_reports/r1/6r1a | HTTPS FTP |
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-Related structure data
Related structure data | 6r0qC 6r0sC 6r0uC 6r0vC 6r11C 6r12C 6r13C 6r18C 6r19C 6r1cC 6r1dC 6r1kC 6r1wC 6r1xC 4v2yS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / End auth comp-ID: PRO / End label comp-ID: PRO / Refine code: 0
NCS ensembles :
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-Components
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 13703.577 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Magnetospirillum gryphiswaldense MSR-1 (magnetotactic) Gene: MGR_0879 / Production host: Escherichia coli (E. coli) / References: UniProt: A4TVL0 |
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-Non-polymers , 5 types, 242 molecules
#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-PO4 / #5: Chemical | ChemComp-JP8 / [( | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.8 Å3/Da / Density % sol: 31.48 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / Details: 0.4 m Ammonium phosphate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 14, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.54→49.18 Å / Num. obs: 44027 / % possible obs: 99.5 % / Redundancy: 12.6 % / CC1/2: 1 / Rmerge(I) obs: 0.13 / Net I/σ(I): 10.28 |
Reflection shell | Resolution: 1.54→1.64 Å / Redundancy: 12.1 % / Rmerge(I) obs: 0.82 / Mean I/σ(I) obs: 1.71 / Num. unique obs: 6798 / CC1/2: 0.84 / % possible all: 96.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4v2y Resolution: 1.54→49.18 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.945 / SU B: 3.904 / SU ML: 0.061 / Cross valid method: THROUGHOUT / ESU R: 0.088 / ESU R Free: 0.087 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.635 Å2
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Refinement step | Cycle: LAST / Resolution: 1.54→49.18 Å
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Refine LS restraints |
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